Difference between revisions of "Part:BBa K2934001"
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[[File:Invertase_Reaction.png|500px|thumb|center|figure 1: the enzymatic reaction of Invertase]] | [[File:Invertase_Reaction.png|500px|thumb|center|figure 1: the enzymatic reaction of Invertase]] | ||
− | Invertase is an enzyme that catalyzes the cleavage of sucrose into fructose and glucose. Since cleaving the sucrose is the very first step in the creation of honey, we have chosen to use a variation of invertase that is reported to be highly active, which originates from the mold species <em>Aspergillus niger</em> [1]. This type of invertase has been widely investigated and is known to be relatively stable | + | Invertase is an enzyme that catalyzes the cleavage of sucrose into fructose and glucose. Since cleaving the sucrose is the very first step in the creation of honey, we have chosen to use a variation of invertase that is reported to be highly active, which originates from the mold species <em>Aspergillus niger</em> [1]. This type of invertase has been widely investigated and is known to be relatively stable [2]. This invertase works as a dimer [3], each monomer the size of 75 kDa (4) and its optimal pH and temperature are 5 and 60⁰C respectively [3]. |
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===References=== | ===References=== |
Revision as of 16:11, 10 October 2019
Invertase-Histag A. niger optimized for B. subtilis
Codes for Invertase enzyme, originally from A. niger, optimized for B. subtilis. The Invertase enzyme catalyzes the degradation of sucrose to glucose and fructose.
Usage and Biology
Invertase is an enzyme that catalyzes the cleavage of sucrose into fructose and glucose. Since cleaving the sucrose is the very first step in the creation of honey, we have chosen to use a variation of invertase that is reported to be highly active, which originates from the mold species Aspergillus niger [1]. This type of invertase has been widely investigated and is known to be relatively stable [2]. This invertase works as a dimer [3], each monomer the size of 75 kDa (4) and its optimal pH and temperature are 5 and 60⁰C respectively [3].
References
[1] Nadeem H, Rashid MH, Siddique MH, Azeem F, Muzammil S, Javed MR, Ali MA, Rasul I, Riaz M. 2015. Microbial invertases: A review on kinetics, thermodynamics, physiochemical properties. Process Biochem 50:1202–1210.
[2] Persano Oddo L, Piazza MG, Pulcini P. 1999. Invertase activity in honey. Apidologie 30:57–65.
[3] L’Hocine L, Wang Z, Jiang B, Xu S. 2000. Purification and partial characterization of fructosyltransferase and invertase from Aspergillus niger AS0023. J Biotechnol 81:73–84.
[4] Goosen C, Yuan XL, Van Munster JM, Ram AFJ, Van Der Maarel MJEC, Dijkhuizen L. 2007. Molecular and biochemical characterization of a novel intracellular invertase from Aspergillus niger with transfructosylating activity. Eukaryot Cell 6:674–681.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 863
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 1168
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 469
Illegal BsaI.rc site found at 811
Illegal SapI.rc site found at 1071